Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.

TitleCryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.
Publication TypeJournal Article
Year of Publication2019
AuthorsGu, J, Zhang, L, Zong, S, Guo, R, Liu, T, Yi, J, Wang, P, Zhuo, W, Yang, M
JournalScience
Volume364
Issue6445
Pagination1068-1075
Date Published2019 06 14
ISSN1095-9203
Abstract

The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo-electron microscopy method. Two classical V-shaped ATP synthase dimers lie antiparallel to each other to form an H-shaped ATP synthase tetramer, as viewed from the matrix. ATP synthase inhibitory factor subunit 1 (IF1) is a well-known in vivo inhibitor of mammalian ATP synthase at low pH. Two IF1 dimers link two ATP synthase dimers, which is consistent with the ATP synthase tetramer adopting an inhibited state. Within the tetramer, we refined structures of intact ATP synthase in two different rotational conformations at 3.34- and 3.45-Å resolution.

DOI10.1126/science.aaw4852
Alternate JournalScience
Citation Key10.1126/science.aaw4852
PubMed ID31197009